P67870 (CSK2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Casein kinase II subunit beta
Short name=CK II beta

Alternative name(s):
Phosvitin
Protein G5a

Gene names

Name:	CSNK2B
Synonyms:	CK2N, G5A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in Wnt signaling By similarity. Plays a complex role in regulating the basal catalytic activity of the alpha subunit. Ref.14 Ref.17
Subunit structure	Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. The beta subunit dimerization is mediated by zinc ions. Interacts with TCTEX1D3 By similarity. Interacts with CD163. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Interacts with MUSK; mediates phosphorylation of MUSK by CK2. Ref.13 Ref.14 Ref.15 Ref.17 Ref.23 Ref.24
Post-translational modification	Phosphorylated by alpha subunit. Ref.12 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
Sequence similarities	Belongs to the casein kinase 2 subunit beta family.
Sequence caution	The sequence CAI18393.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW adiponectin-mediated signaling pathway Inferred from direct assay. Source: BHF-UCL axon guidance Traceable author statement. Source: Reactome cellular protein complex assembly Non-traceable author statement. Source: BHF-UCL negative regulation of cell proliferation Traceable author statement. Source: BHF-UCL regulation of DNA binding Non-traceable author statement. Source: BHF-UCL
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: UniProtKB protein kinase CK2 complex Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct protein domain specific binding Inferred from physical interaction. Source: UniProtKB protein kinase regulator activity Non-traceable author statement Ref.1. Source: UniProtKB receptor binding Inferred from physical interaction. Source: BHF-UCL transcription factor binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		6	EBI-348169,EBI-348169
CBX4	O00257-3	2	EBI-348169,EBI-4392727
CSNK2A1	P68400	10	EBI-348169,EBI-347804
CSNK2A2	P19784	4	EBI-348169,EBI-347451

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

Casein kinase II subunit beta

PRO_0000068236

Regions

Region

188 – 193

6

Interaction with alpha subunit By similarity

Compositional bias

55 – 64

10

Asp/Glu-rich (acidic)

Sites

Metal binding

109

1

Zinc

Metal binding

114

1

Zinc

Metal binding

137

1

Zinc

Metal binding

140

1

Zinc

Amino acid modifications

Modified residue

2

1

Phosphoserine; by autocatalysis Ref.16 Ref.19 Ref.20

Modified residue

3

1

Phosphoserine Ref.16 Ref.19 Ref.20

Modified residue

4

1

Phosphoserine Ref.16 Ref.19 Ref.20

Modified residue

8

1

Phosphoserine Ref.19 Ref.20

Modified residue

69

1

Phosphoserine Ref.19 Ref.20

Modified residue

145

1

Phosphothreonine Ref.20

Modified residue

197

1

Phosphotyrosine Ref.20

Modified residue

205

1

Phosphoserine Ref.20

Modified residue

209

1

Phosphoserine Ref.16 Ref.18 Ref.19 Ref.20

Modified residue

212

1

N6-acetyllysine Ref.21

Experimental info

Sequence conflict

194

1

P → A in AAA52123. Ref.3

Secondary structure

1

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215

Helix Strand Turn

Details...

Helix

9 – 15

7

Helix

27 – 31

5

Helix

33 – 36

4

Helix

39 – 41

3

Helix

46 – 53

8

Helix

67 – 87

21

Helix

91 – 102

12

Turn

103 – 106

4

Helix

112 – 114

3

Beta strand

120 – 122

3

Beta strand

134 – 136

3

Turn

138 – 140

3

Helix

149 – 151

3

Helix

156 – 158

3

Helix

163 – 170

8

Helix

172 – 174

3

Beta strand

195 – 197

3

Sequences

	Sequence		Length	Mass (Da)
	P67870 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: E465B1E699B0E0EC	FASTA	215	24,942
	10 20 30 40 50 60 MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE 70 80 90 100 110 120 ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML 130 140 150 160 170 180 PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA 190 200 210 NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta." Jakobi R., Voss H., Pyerin W. Eur. J. Biochem. 183:227-233(1989) [PubMed: 2666134] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells." Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L., Wood C.M., Moses R.E., Canaani D. Mutat. Res. 236:85-97(1990) [PubMed: 1694965] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II." Heller-Harrison R.A., Meisner H., Czech M.P. Biochemistry 28:9053-9058(1989) [PubMed: 2513884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure of the gene encoding human casein kinase II subunit beta." Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J., Ansorge W., Pyerin W. J. Biol. Chem. 266:13706-13711(1991) [PubMed: 1856204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Sequencing of full-length cDNA encoding the alpha and beta subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIalpha intronless gene in a megakaryocytic cell line." Singh L.S., Kalafatis M. Biochemistry 41:8935-8940(2002) [PubMed: 12102635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed: 14656967] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[12]	"Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit." Ackerman P., Glover C.V., Osheroff N. Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990) [PubMed: 2300566] [Abstract] Cited for: PHOSPHORYLATION.
[13]	"Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C." Ritter M., Buechler C., Kapinsky M., Schmitz G. Eur. J. Immunol. 31:999-1009(2001) [PubMed: 11298324] [Abstract] Cited for: INTERACTION WITH CD163.
[14]	"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1." Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H. Mol. Cell 7:283-292(2001) [PubMed: 11239457] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
[15]	"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex." Keller D.M., Lu H. J. Biol. Chem. 277:50206-50213(2002) [PubMed: 12393879] [Abstract] Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
[16]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; SER-4 AND SER-209, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction." Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S. Genes Dev. 20:1800-1816(2006) [PubMed: 16818610] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MUSK, INTERACTION WITH MUSK.
[18]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; SER-4; SER-8; SER-69 AND SER-209, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; SER-4; SER-8; SER-69; THR-145; TYR-197; SER-205 AND SER-209, MASS SPECTROMETRY.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, MASS SPECTROMETRY.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization." Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J., Chambaz E.M., Cochet C., Dideberg O. EMBO J. 18:2930-2940(1999) [PubMed: 10357806] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, ZINC-BINDING SITES.
[24]	"Crystallization and preliminary characterization of crystals of human protein kinase CK2." Niefind K., Guerra B., Ermakowa I., Issinger O.G. Acta Crystallogr. D 56:1680-1684(2000) [PubMed: 11092945] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16937 mRNA. Translation: CAA34811.1.
X16312 mRNA. Translation: CAA34379.1.
M30448 mRNA. Translation: AAA52123.1.
X57152 Genomic DNA. Translation: CAA40442.1.
AY113186 mRNA. Translation: AAM50092.1.
CR541699 mRNA. Translation: CAG46500.1.
AF129756 Genomic DNA. Translation: AAD18081.1.
BA000025 Genomic DNA. Translation: BAB63386.1.
DQ314868 Genomic DNA. Translation: ABC40727.1.
AL662899 Genomic DNA. Translation: CAI96141.1.
AL662899 Genomic DNA. Translation: CAI18393.2. Different initiation.
AL670886 Genomic DNA. Translation: CAI17800.1.
AL805934 Genomic DNA. Translation: CAI18523.1.
BC112017 mRNA. Translation: AAI12018.1.
BC112019 mRNA. Translation: AAI12020.1.

IPI

IPI00010865.

PIR

A39459.

RefSeq

NP_001311.3. NM_001320.5.

UniGene

Hs.73527.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DS5	X-ray	3.16	E/F/G/H	181-203	[»]
1JWH	X-ray	3.10	C/D	1-215	[»]
1QF8	X-ray	1.74	A/B	1-182	[»]
3EED	X-ray	2.80	A/B	1-193	[»]

ProteinModelPortal

P67870.

SMR

P67870. Positions 2-205.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-131N.

IntAct

P67870. 57 interactions.

MINT

MINT-88683.

STRING

P67870.

Polymorphism databases

DMDM

54037520.

Proteomic databases

PRIDE

P67870.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375865; ENSP00000365025; ENSG00000204435.
ENST00000375866; ENSP00000365026; ENSG00000204435.
ENST00000375882; ENSP00000365042; ENSG00000204435.
ENST00000375885; ENSP00000365046; ENSG00000204435.

GeneID

1460.

KEGG

hsa:1460.

UCSC

uc003nvr.1. human.

Organism-specific databases

CTD

1460.

GeneCards

GC06P031633.

HGNC

HGNC:2460. CSNK2B.

HPA

CAB004349.
CAB013087.
CAB016059.
HPA005944.

MIM

115441. gene.

neXtProt

NX_P67870.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13612.

GeneTree

ENSGT00390000003781.

HOVERGEN

HBG051131.

InParanoid

P67870.

OrthoDB

EOG4FBHTQ.

PhylomeDB

P67870.

Enzyme and pathway databases

Pathway_Interaction_DB

nfkappabatypicalpathway. Atypical NF-kappaB pathway.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

CleanEx

HS_CSNK2B.

Genevestigator

P67870.

GermOnline

ENSG00000204435. Homo sapiens.

Family and domain databases

InterPro

IPR016149. Casein_kin_II_reg-sub_a-hlx.
IPR016150. Casein_kin_II_reg-sub_b-sht.
IPR000704. Casein_kinase_II_reg-sub.
[Graphical view]

Gene3D

G3DSA:1.10.1820.10. Casein_kin_II_reg-sub_a-hlx. 1 hit.
G3DSA:2.20.25.20. Casein_kin_II_reg-sub_b-sht. 1 hit.

KO

K03115.

PANTHER

PTHR11740. CAS_kinase_II. 1 hit.

Pfam

PF01214. CK_II_beta. 1 hit.
[Graphical view]

PRINTS

PR00472. CASNKINASEII.

SMART

SM01085. CK_II_beta. 1 hit.
[Graphical view]

SUPFAM

SSF57798. Casein_kinase_II_reg-sub. 1 hit.

PROSITE

PS01101. CK2_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

6001.

SOURCE

Search...

Entry information

Entry name

CSK2B_HUMAN

Accession

Primary (citable) accession number: P67870
Secondary accession number(s): P07312, P13862, Q4VX47

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.